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1rgv
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1rgv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rgv, resolution 2.90Å" /> '''Crystal Structure of...) |
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| - | [[Image:1rgv.gif|left|200px]]<br /><applet load="1rgv" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1rgv, resolution 2.90Å" /> | ||
| - | '''Crystal Structure of the Ferredoxin from Thauera aromatica'''<br /> | ||
| - | == | + | ==Crystal Structure of the Ferredoxin from Thauera aromatica== |
| - | 4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a central enzyme in the | + | <StructureSection load='1rgv' size='340' side='right'caption='[[1rgv]], [[Resolution|resolution]] 2.90Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1rgv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thauera_aromatica_K172 Thauera aromatica K172]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RGV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgv OCA], [https://pdbe.org/1rgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rgv RCSB], [https://www.ebi.ac.uk/pdbsum/1rgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rgv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O88151_THAAR O88151_THAAR] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/1rgv_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rgv ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a central enzyme in the metabolism of phenolic compounds in anaerobic bacteria. The enzyme catalyzes the reductive removal of the phenolic hydroxyl group from 4-hydroxybenzoyl-CoA, yielding benzoyl-CoA and water. 4-HBCR belongs to the xanthine oxidase (XO) family of molybdenum enzymes which occur as heterodimers, (alphabetagamma)(2). 4-HBCR contains two molybdopterins, four [2Fe-2S] and two [4Fe-4S] clusters and two FADs. A low-potential Allochromatium vinosum-type ferredoxin containing two [4Fe-4S] clusters serves as an in vivo electron donor for 4-HBCR. In this work, the oxygen-sensitive proteins 4-HBCR and the ferredoxin (TaFd) from Thauera aromatica were crystallized under anaerobic conditions. 4-HBCR crystallized with PEG 4000 and MPD as precipitant diffracted to about 1.6 A resolution and the crystals were highly suitable for X-ray structure analysis. Crystals of TaFd were obtained with (NH(4))(3)PO(4) as precipitant and revealed a solvent content of 77%, which is remarkably high for a small soluble protein. The structure of TaFd was solved at 2.9 A resolution by the molecular-replacement method using the highly related structure of the ferredoxin (CvFd) from A. vinosum as a model. Structural changes between the two ferredoxins around the [4Fe-4S] cluster can be correlated with their different redox potentials. | ||
| - | + | Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin.,Unciuleac M, Boll M, Warkentin E, Ermler U Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):388-91. Epub 2004, Jan 23. PMID:14747735<ref>PMID:14747735</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1rgv" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thauera aromatica K172]] | ||
| + | [[Category: Boll M]] | ||
| + | [[Category: Ermler U]] | ||
| + | [[Category: Unciuleac M]] | ||
| + | [[Category: Warkentin E]] | ||
Current revision
Crystal Structure of the Ferredoxin from Thauera aromatica
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